We provide a system for the mass production of target proteins and peptides (transforming cells, purified proteins and peptides), using (a) the mechanism of biosynthesis, both production and repression (feedback inhibition), that a cultured cell system (e.g. Tobacco BY-II cells) of higher plants possesses, and (b) the plant virus mechanism controlling silencing of the host cells ( e.g. Tobacco BY-II cells).
Since this system makes use of higher plant cells, its products can be cultured using nutrient solutions based on inorganic salt. The system also makes possible post-translational modification of phosphorylation and glycosylation and the construction of protein-folding conformation, which would be difficult with the technologies that make use of microorganisms such as Escherichia coli (E. Coli) and yeasts.
This system produces mass-produced cells from cloned target proteins and peptides.
- Examples of the proteins that are produced with the system include
- jellyfish-based green fluorescent proteins (GFP)
- E. Coli-based dihydrofolate reductase
- CPI-17 protein functional domain gene
- single strand antibody gene
- calmodulin genes
- plant-based lectin
- Mass-Production of Target Proteins and Peptides
- Low Cost for Production(Medium, Incubation Facility)
- Production of Eucaryotic-Proteins(Post-Translational Modification, e.g. Phosphorylation and Glycosylation, and Folding
- Easy Purification of Target Proteins and Peptides
Expression of Green Fluorescent Protein(GFP) Originating in Jellyfish(Observation under Fluorescence Microscope)
Expression of Green Fluorescent Protein(GFP) Originating in Jellyfish
Expression and Physiological Activity of Dihydro Folic Acid Reductase(DHFR)
Expression of Human Gamma Interferon(hIFNγ) in Transgenic Tobacco Cells
(Detected by Western Blotting)